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Journal articles
Human Natural Antibodies Recognizing Glycan Galβ1-3GlcNAc (LeC)
Abstract : The level of human natural antibodies of immunoglobulin M isotype against LeC in patients with breast cancer is lower than in healthy women. The epitope specificity of these antibodies has been characterized using a printed glycan array and enzyme-linked immunosorbent assay (ELISA), the antibodies being isolated from donors' blood using LeC-Sepharose (LeC is Galβ1-3GlcNAcβ). The isolated antibodies recognize the disaccharide but do not bind to glycans terminated with LeC, which implies the impossibility of binding to regular glycoproteins of non-malignant cells. The avidity (as dissociation constant value) of antibodies probed with a multivalent disaccharide is 10-9 M; the nanomolar level indicates that the concentration is sufficient for physiological binding to the cognate antigen. Testing of several breast cancer cell lines showed the strongest binding to ZR 75-1. Interestingly, only 7% of the cells were positive in a monolayer with a low density, increasing up to 96% at highest density. The enhanced interaction (instead of the expected inhibition) of antibodies with ZR 75-1 cells in the presence of Galβ1-3GlcNAcβ disaccharide, indicates that the target epitope of anti-LeC antibodies is a molecular pattern with a carbohydrate constituent rather than a glycan.
Cited literature [21 references]
https://www.hal.inserm.fr/inserm-02948773
Contributor : Elizabeth Bernardo <>
Submitted on : Friday, September 25, 2020 - 9:15:56 AM
Last modification on : Tuesday, January 19, 2021 - 9:28:25 AM
Long-term archiving on: : Thursday, December 3, 2020 - 5:31:12 PM
Contributor : Elizabeth Bernardo <>
Submitted on : Friday, September 25, 2020 - 9:15:56 AM
Last modification on : Tuesday, January 19, 2021 - 9:28:25 AM
Long-term archiving on: : Thursday, December 3, 2020 - 5:31:12 PM
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ijms-21-06511-v2.pdf
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